1TR0
Crystal Structure of a boiling stable protein SP1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL9-2 |
Synchrotron site | SSRL |
Beamline | BL9-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2002-04-28 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.954 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 97.028, 94.750, 168.029 |
Unit cell angles | 90.00, 90.11, 90.00 |
Refinement procedure
Resolution | 48.500 - 1.800 |
R-factor | 0.16447 |
Rwork | 0.162 |
R-free | 0.20192 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1si9 |
RMSD bond length | 0.017 |
RMSD bond angle | 1.588 |
Data scaling software | CCP4 ((SCALA)) |
Phasing software | MOLREP |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.500 | 1.900 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.447 | |
Number of reflections | 246060 | |
<I/σ(I)> | 2.8 | |
Completeness [%] | 92.5 | 88.4 |
Redundancy | 1.9 | 1.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | PEG 3000, Sodium Chloride, Hepes, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |